4BEB
MUTANT (K220E) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP
Replaces: 2Y3TFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0004519 | molecular_function | endonuclease activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006304 | biological_process | DNA modification |
A | 0009035 | molecular_function | type I site-specific deoxyribonuclease activity |
A | 0009307 | biological_process | DNA restriction-modification system |
B | 0003677 | molecular_function | DNA binding |
B | 0004519 | molecular_function | endonuclease activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006304 | biological_process | DNA modification |
B | 0009035 | molecular_function | type I site-specific deoxyribonuclease activity |
B | 0009307 | biological_process | DNA restriction-modification system |
C | 0003677 | molecular_function | DNA binding |
C | 0004519 | molecular_function | endonuclease activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006304 | biological_process | DNA modification |
C | 0009035 | molecular_function | type I site-specific deoxyribonuclease activity |
C | 0009307 | biological_process | DNA restriction-modification system |
D | 0003677 | molecular_function | DNA binding |
D | 0004519 | molecular_function | endonuclease activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006304 | biological_process | DNA modification |
D | 0009035 | molecular_function | type I site-specific deoxyribonuclease activity |
D | 0009307 | biological_process | DNA restriction-modification system |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 1885 |
Chain | Residue |
A | THR314 |
A | ASP408 |
A | ATP1886 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ATP A 1886 |
Chain | Residue |
A | THR309 |
A | GLY310 |
A | SER311 |
A | GLY312 |
A | LYS313 |
A | THR314 |
A | LEU315 |
A | THR661 |
A | GLY662 |
A | ASP664 |
A | ARG688 |
A | ARG691 |
A | MG1885 |
A | MET227 |
A | LEU270 |
A | VAL271 |
A | MET272 |
A | ARG273 |
A | GLN276 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 1885 |
Chain | Residue |
B | THR314 |
B | ASP408 |
B | ATP1886 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ATP B 1886 |
Chain | Residue |
B | LEU270 |
B | VAL271 |
B | MET272 |
B | ARG273 |
B | GLN276 |
B | THR309 |
B | GLY310 |
B | SER311 |
B | GLY312 |
B | LYS313 |
B | THR314 |
B | LEU315 |
B | THR661 |
B | GLY662 |
B | ASP664 |
B | ARG688 |
B | ARG691 |
B | MG1885 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 1885 |
Chain | Residue |
C | THR314 |
C | ASP408 |
C | ATP1886 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ATP C 1886 |
Chain | Residue |
C | MET227 |
C | LEU270 |
C | VAL271 |
C | MET272 |
C | ARG273 |
C | GLN276 |
C | THR309 |
C | GLY310 |
C | SER311 |
C | GLY312 |
C | LYS313 |
C | THR314 |
C | LEU315 |
C | THR661 |
C | GLY662 |
C | ASP664 |
C | ARG688 |
C | ARG691 |
C | MG1885 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG D 1885 |
Chain | Residue |
D | THR314 |
D | ASP408 |
D | GLU409 |
D | ATP1886 |
site_id | AC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ATP D 1886 |
Chain | Residue |
D | MET227 |
D | LEU270 |
D | VAL271 |
D | MET272 |
D | ARG273 |
D | GLN276 |
D | THR309 |
D | GLY310 |
D | SER311 |
D | GLY312 |
D | LYS313 |
D | THR314 |
D | THR661 |
D | GLY662 |
D | ASP664 |
D | ARG688 |
D | ARG691 |
D | MG1885 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541 |
Chain | Residue | Details |
A | HIS307 | |
B | HIS307 | |
C | HIS307 | |
D | HIS307 |